
%0 Journal Article
%A Zanacchi, RM 
%A Moore, WJ 
%T Temperature and pH dependence of proton N.M.R. of glutamine in peptides
%J Australian Journal of Chemistry
%D 1980/07/01
%V 33
%N 7
%P 1505-1510
%K 
%R https://doi.org/10.1071/CH9801505
%U https://www.publish.csiro.au/paper/CH9801505 
%X The proton n.m.r. spectra of the peptides Ala-Glu-Gly-Gln-Gly and Gly- Gln-Gly as measured in dimethyl sulfoxide over a range of temperatures yielded kinetic parameters for rotation about the carbon-nitrogen bonds of the glutamine side chains of &#916;H&#8225; 71.6 kJ mol-1, &#916;S&#8225; 2.1 J mol-1 K-1, and &#916;H&#8225;/70.6 kJ mol-1, &#916;S&#8225; -0.5 J mol-1 K-1, respectively, at 298 K. On pH titration in dimethyl sulfoxide/water solutions, the chemical shifts of the cis protons of the glutamine amide remained constant whereas those of the trans protons were altered with a pK corresponding to that of the terminal glycine. 
